Molecular Cloning and Characterization of a Broad Substrate Terpenoid Oxidoreductase from Artemisia annua

被引：11

作者：

Ryden, Anna-Margareta ^{[2
]}

Ruyter-Spira, Carolien ^{[1
]}

Litjens, Ralph ^{[1
]}

Takahashi, Shunji ^{[3
]}

Quax, Wim ^{[2
]}

Osada, Hiroyuki ^{[3
]}

Bouwmeester, Harro ^{[1
,4
]}

Kayser, Oliver ^{[2
]}

机构：

[1] Plant Res Int, NL-6700 AA Wageningen, Netherlands

[2] Univ Groningen, GUIDE, Dept Pharmaceut Biol, NL-9713 AV Groningen, Netherlands

[3] RIKEN, Dept Biol Chem, Saitama 3560004, Japan

[4] Wageningen Univ, Lab Plant Physiol, NL-6700 AR Wageningen, Netherlands

来源：

PLANT AND CELL PHYSIOLOGY | 2010年 / 51卷 / 07期

关键词：

Artemisia annua L; Menthone; Oxidoreductase; red1; Terpenoids; AMORPHA-4,11-DIENE SYNTHASE; FUNCTIONAL ASSIGNMENTS; BIOSYNTHETIC-PATHWAY; KEY ENZYME; EXPRESSION; REDUCTASE; ACID;

D O I：

10.1093/pcp/pcq073

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

From Artemisia annua L., a new oxidoreductase (Red 1) was cloned, sequenced and functionally characterized. Through bioinformatics, heterologous protein expression and enzyme substrate conversion assays, the elucidation of the enzymatic capacities of Red1 was achieved. Red1 acts on monoterpenoids, and in particular functions as a menthone:neomenthol oxidoreductase. The kinetic parameter k(cat)/K-m was determined to be 939-fold more efficient for the reduction of (-)-menthone to (+)-neomenthol than results previously reported for the menthone: neomenthol reductase from Menthaxpiperita. Based on its kinetic properties, the possible use of Red1 in biological crop protection is discussed.

引用

页码：1219 / 1228

页数：10

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